A multi-protein complex controls cAMP signalling and filamentation in the fungal pathogen Candida albicans

Candida albicans is an opportunistic fungal pathogen of humans. The ability of the fungus to grow as both yeast and filamentous forms is essential for its pathogenicity. Morphogenesis of C. albicans is largely regulated through the secondary messenger cAMP, produced by the soluble adenylyl cyclase, Cyr1p. Recent evidence suggests that Cyr1p can be directly stimulated by environmental cues to increase cytoplasmic cAMP levels and thus promote hyphal development. In this issue of Molecular Microbiology, Zou et al. demonstrate that, in response to some environmental cues, Cyr1p functions as part of a tripartite complex additionally involving Cap1p and G-actin. All three proteins in the complex are required to raise cytosolic cAMP levels after stimulation with serum and bacterial peptidoglycan. The formation of such a complex highlights the importance of precise regulation of Cyr1p activity in response to host environmental cues.